The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
An NMDA Receptor ER Retention Signal Regulated by Phosphorylation and Alternative Splicing
Open accessAbstract
Formation of mature excitatory synapses requires the assembly and delivery of NMDA receptors to the neuronal plasma membrane. A key step in the trafficking of NMDA receptors to synapses is the exit of newly assembled receptors from the endoplasmic reticulum (ER). Here we report the identification of an RXR-type ER retention/retrieval motif in the C-terminal tail of the NMDA receptor subunit NR1 that regulates receptor surface expression in heterologous cells and in neurons. In addition, we show that PKC phosphorylation and an alternatively spliced consensus type I PDZ-binding domain suppress ER retention. These results demonstrate a novel quality control function for alternatively spliced C-terminal domains of NR1 and implicate both phosphorylation and potential PDZ-mediated interactions in the trafficking of NMDA receptors through early stages of the secretory pathway.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Long-Term Potentiation--A Decade of Progress?
Malenka, R. C., & Nicoll, A. R. A. (1999) · Science · doi:10.1126/science.285.5435.1870 · Cited by 2,729
Heteromeric NMDA receptors: molecular and functional distinction of subtypes
Monyer, H., Sprengel, R., Schoepfer, R., Herb, A., Higuchi, M., Lomeli, H., Burnashev, N., Sakmann, B., & Seeburg, P. H. (1992) · Science · doi:10.1126/science.256.5060.1217 · Cited by 2,541
Domain Interaction Between NMDA Receptor Subunits and the Postsynaptic Density Protein PSD-95
Kornau, H., Schenker, L. T., Kennedy, M. B., & Seeburg, P. H. (1995) · Science · doi:10.1126/science.7569905 · Cited by 1,916
Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains
Songyang, Z., Fanning, A. S., Fu, C., Xu, J., Marfatia, S. M., Chishti, A. H., Crompton, A., Chan, A. C., Anderson, J. M., & Cantley, L. C. (1997) · Science · doi:10.1126/science.275.5296.73 · Cited by 1,385
Setting the Standards: Quality Control in the Secretory Pathway
Ellgaard, L., Molinari, M., & Helenius, A. (1999) · Science · doi:10.1126/science.286.5446.1882 · Cited by 1,192
Glutamate receptors in the mammalian central nervous system
Ozawa, S., Kamiya, H., & Tsuzuki, K. (1998) · Progress in Neurobiology · doi:10.1016/s0301-0082(97)00085-3 · Cited by 1,133
Deglycosylation of asparagine-linked glycans by peptide:N-glycosidase F
Tarentino, A. L., Gomez, C. M., & Plummer, T. H. (1985) · Biochemistry · doi:10.1021/bi00338a028 · Cited by 1,130
A New ER Trafficking Signal Regulates the Subunit Stoichiometry of Plasma Membrane KATP Channels
Zerangue, N., Schwappach, B., Jan, Y. N., & Jan, L. Y. (1999) · Neuron · doi:10.1016/s0896-6273(00)80708-4 · Cited by 1,025
Protein kinase C reduces Mg2+ block of NMDA-receptor channels as a mechanism of modulation
Chen, L., & Huang, L.-Y. M. (1992) · Nature · doi:10.1038/356521a0 · Cited by 974
Kinesin Superfamily Motor Protein KIF17 and mLin-10 in NMDA Receptor-Containing Vesicle Transport
Setou, M., Nakagawa, T., Seog, D., & Hirokawa, N. (2000) · Science · doi:10.1126/science.288.5472.1796 · Cited by 727
Cited by
Sorted by citations
Items 401–418 of 418
Regulation of the TRP calcium channel by eye‐PKC in Drosophila
Popescu, D. C., & Shieh, B. (2006) · The FASEB Journal · doi:10.1096/fasebj.20.4.a495-c
Alternative splicing of GluN1 gates glycine-primed internalization of NMDA receptorsPreprint
Li, H., Rajani, V., Han, L., Chung, D., Cooke, J. E., Sengar, A. S., & Salter, M. W. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.18.423454
Faculty Opinions recommendation of Structure, function, and allosteric modulation of NMDA receptors.
Peoples, R. W. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733689357.793549023
Gibb, A. J. (2019) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0000254.pub3
Molecular Determinants of Spinal Hyperexcitability in Rat and Human Models of Pathological Pain
Dedek, A. (2021) · Carleton University's Institutional Repository (MacOdrum Library, Carleton University) · doi:10.22215/etd/2021-14590
Heuser, J. E. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.22.489201
Intracellular regulation of a serotonin-gated ion channel links receptor trafficking to memory
Cesar, L. C., Zabeo, D., Cellini, A., Aspholm, E. E., Kolsrud, A., Panagaki, D., Höög, J. L., & Morud, J. (2026) · iScience · doi:10.1016/j.isci.2026.117309
Netolický, J., Lee, S., Zahumenska, P., Kolcheva, M., Misiachna, A., Rehakova, K., Kortus, Š., Song, J., Hemelíková, K., Langore, E., et al. (2026) · Journal of Neuroscience · doi:10.1523/jneurosci.0409-25.2026
Jézéquel, J. (2016) · theses.fr (ABES) · doi:10.70675/a7276087zc049z442fz8b5bzab9e03d034cb
Super-resolution imaging reveals differential organization and regulation of NMDA receptor subtypes
Kellermayer, B. (2018) · theses.fr (ABES) · doi:10.70675/53ab72bcz0d7cz42d6z8567z069d3489d10e
Fourneau, J. (2018) · theses.fr (ABES) · doi:10.70675/6324f6b7z65d0z4f8aza022zfaaa24669376
Impact of open channel blockers on the surface dynamics and organization of NMDA receptors
Fernandes, A. (2020) · theses.fr (ABES) · doi:10.70675/d12c14b2z7a80z4668z9c48z8e2c0e41c009 · Cited by 1
Hunter, D. (2023) · theses.fr (ABES) · doi:10.70675/ae0cf321z922dz4431z8e9czca6cbf457b2e
Molecular impact of anti-NMDA receptor autoantibodies
Jamet, Z. (2023) · theses.fr (ABES) · doi:10.70675/87243db0za802z49e1zbd1ez607bb3d60120
Molecular mechanisms underlying the surface organization of the NMDA receptors during development
Bénac, N. (2024) · theses.fr (ABES) · doi:10.70675/e3508a2ezb62ez4f99zb27bz156201271974
Glutamate Receptors: NMDA and Delta Receptors
Yuzaki, M. (2009) · Springer eBooks · doi:10.1007/978-0-387-30370-3_16
Postsynaptic Transport Packets
Washbourne, P. (2006) · Springer eBooks · doi:10.1007/978-0-387-32562-0_15
Metadata
- Authors
- Scott, D. B., Blanpied, T. A., Swanson, G. T., Zhang, C., & Ehlers, M. D.
- Affiliations
- Duke Medical Center (US)
- Salk Institute for Biological Studies (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2001-05-01
- Volume
- 21
- Issue
- 9
- Pages
- 3063-3072
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6762585
- OpenAlex
- W1527134354
- Cited by
- 418
- References
- 62
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 5 · 2023: 5 · 2022: 10 · 2021: 10 · 2020: 10 · 2019: 8 · 2018: 11 · 2017: 10 · 2016: 3 · 2015: 12 · 2014: 13 · 2013: 10 · 2012: 10
- FWCI
- 12.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alfred P. Sloan Foundation
- American Health Assistance Foundation
- McKnight Foundation
- North Carolina Biotechnology Center
- Triangle Community Foundation
- National Alliance for Research on Schizophrenia and Depression
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (R01 NS39402, R01NS039402)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- NMDA receptor, NR1 subunit, endoplasmic reticulum retention signal, PKC phosphorylation, alternative splicing, PDZ-binding domain, receptor surface expression, excitatory synapse formation, secretory pathway, quality control, receptor trafficking
- MeSH terms
- Animals, Cells, Cultured, Endoplasmic Reticulum, Hippocampus, Humans, Neurons, Phosphorylation, Protein Kinase C, Recombinant Fusion Proteins, Transcription Factors, Transfection, Receptors, Interleukin-2, Receptors, N-Methyl-D-Aspartate, Alternative Splicing, Protein Structure, Tertiary, Receptors, Retinoic Acid, Amino Acid Motifs, Protein Subunits, Protein Sorting Signals, Retinoid X Receptors, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
